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P09626 (ATP4A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium-transporting ATPase alpha chain 1

EC=3.6.3.10
Alternative name(s):
Gastric H(+)/K(+) ATPase subunit alpha
Proton pump
Gene names
Name:Atp4a
Synonyms:Hka
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1033 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. Responsible for acid production in the stomach.

Catalytic activity

ATP + H2O + H+(In) + K+(Out) = ADP + phosphate + H+(Out) + K+(In).

Subunit structure

Composed of two subunits: alpha (catalytic) and beta.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10331032Potassium-transporting ATPase alpha chain 1
PRO_0000046257

Regions

Topological domain2 – 9695Cytoplasmic Potential
Transmembrane97 – 11721Helical; Potential
Topological domain118 – 14023Lumenal Potential
Transmembrane141 – 16121Helical; Potential
Topological domain162 – 297136Cytoplasmic Potential
Transmembrane298 – 31720Helical; Potential
Topological domain318 – 32912Lumenal Potential
Transmembrane330 – 34718Helical; Potential
Topological domain348 – 781434Cytoplasmic Potential
Transmembrane782 – 80120Helical; Potential
Topological domain802 – 81110Lumenal Potential
Transmembrane812 – 83221Helical; Potential
Topological domain833 – 85220Cytoplasmic Potential
Transmembrane853 – 87523Helical; Potential
Topological domain876 – 92752Lumenal Potential
Transmembrane928 – 94720Helical; Potential
Topological domain948 – 96114Cytoplasmic Potential
Transmembrane962 – 98019Helical; Potential
Topological domain981 – 99515Lumenal Potential
Transmembrane996 – 101621Helical; Potential
Topological domain1017 – 103317Cytoplasmic Potential

Sites

Active site38514-aspartylphosphate intermediate By similarity
Metal binding7261Magnesium By similarity
Metal binding7301Magnesium By similarity

Amino acid modifications

Modified residue61Phosphotyrosine By similarity
Modified residue91Phosphotyrosine By similarity
Modified residue261Phosphoserine By similarity
Modified residue9521Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict31K → KA in AAA72354. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P09626 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5A8835BA0CAF987E

FASTA1,033114,038
        10         20         30         40         50         60 
MGKENYELYS VELGTGPGGD MAAKMSKKKA GGGGGKKKEK LENMKKEMEM NDHQLSVSEL 

        70         80         90        100        110        120 
EQKYQTSATK GLKASLAAEL LLRDGPNALR PPRGTPEYVK FARQLAGGLQ CLMWVAAAIC 

       130        140        150        160        170        180 
LIAFAIQASE GDLTTDDNLY LALALIAVVV VTGCFGYYQE FKSTNIIASF KNLVPQQATV 

       190        200        210        220        230        240 
IRDGDKFQIN ADQLVVGDLV EMKGGDRVPA DIRILSAQGC KVDNSSLTGE SEPQTRSPEC 

       250        260        270        280        290        300 
THESPLETRN IAFFSTMCLE GTAQGLVVST GDRTIIGRIA SLASGVENEK TPIAIEIEHF 

       310        320        330        340        350        360 
VDIIAGLAIL FGATFFVVAM CIGYTFLRAM VFFMAIVVAY VPEGLLATVT VCLSLTAKRL 

       370        380        390        400        410        420 
ASKNCVVKNL EAVETLGSTS VICSDKTGTL TQNRMTVSHL WFDNHIHTAD TTEDQSGQTF 

       430        440        450        460        470        480 
DQSSETWRAL CRVLTLCNRA AFKSGQDAVP VPKRIVIGDA SETALLKFSE LTLGNAMGYR 

       490        500        510        520        530        540 
DRFPKVCEIP FNSTNKFQLS IHTLEDPRDP RHLLVMKGAP ERVLERCSSI LIKGQELPLD 

       550        560        570        580        590        600 
EQWREAFQTA YLSLGGLGER VLGFCQLYLN EKDYPPGYTF DVEAMNFPSS GLCFAGLVSM 

       610        620        630        640        650        660 
IDPPRATVPD AVLKCRTAGI RVIMVTGDHP ITAKAIAASV GIISEGSETV EDIAARLRMP 

       670        680        690        700        710        720 
VDQVNKKDAR ACVINGMQLK DMDPSELVEA LRTHPEMVFA RTSPQQKLVI VESCQRLGAI 

       730        740        750        760        770        780 
VAVTGDGVND SPALKKADIG VAMGIAGSDA AKNAADMILL DDNFASIVTG VEQGRLIFDN 

       790        800        810        820        830        840 
LKKSIAYTLT KNIPELTPYL IYITVSVPLP LGCITILFIE LCTDIFPSVS LAYEKAESDI 

       850        860        870        880        890        900 
MHLRPRNPRR DRLVNEPLAA YSYFQIGAIQ SFAGFADYFT AMAQEGWFPL LCVGLRPQWE 

       910        920        930        940        950        960 
DHHLQDLQDS YGQEWTFGQR LYQQYTCYTV FFISIEMCQI ADVLIRKTRR LSAFQQGFFR 

       970        980        990       1000       1010       1020 
NRILVIAIVF QVCIGCFLCY CPGMPNIFNF MPIRFQWWLV PMPFGLLIFV YDEIRKLGVR 

      1030 
CCPGSWWDQE LYY 

« Hide

References

[1]"Molecular cloning of the rat stomach (H+ + K+)-ATPase."
Shull G.E., Lingrel J.B.
J. Biol. Chem. 261:16788-16791(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Shull G.E.
Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Expression and cellular localization of mRNA encoding the 'gastric' isoform of H(+)-K(+)-ATPase alpha-subunit in rat kidney."
Ahn K.Y., Kone B.C.
Am. J. Physiol. 268:F99-F109(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-507.
[4]Song I., Mortell P., Gantz I., Marino L.R., Yamada T.
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
Tissue: Liver.
[5]"Control region and gastric specific transcription of the rat H+,K(+)-ATPase alpha subunit gene."
Oshiman K., Motajima K., Mahmood S., Shimada A., Tamura S., Maeda M., Futai M.
FEBS Lett. 281:250-254(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 177-260 AND 436-466.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02649 mRNA. Translation: AAA66036.1.
S74801 mRNA. Translation: AAP31528.1.
L11569 Genomic DNA. Translation: AAA72354.1.
X61934 Genomic DNA. Translation: CAA43938.1.
X61935 Genomic DNA. Translation: CAA43939.1.
PIRA25344.
UniGeneRn.214529.

3D structure databases

ProteinModelPortalP09626.
SMRP09626. Positions 1-33, 35-1033.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP09626.
ChEMBLCHEMBL2095199.

PTM databases

PhosphoSiteP09626.

Proteomic databases

PaxDbP09626.
PRIDEP09626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2177. rat.

Organism-specific databases

RGD2177. Atp4a.

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265622.
HOVERGENHBG004298.
InParanoidP09626.
PhylomeDBP09626.

Enzyme and pathway databases

BRENDA3.6.3.10. 5301.

Gene expression databases

GenevestigatorP09626.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR015127. ATPase_P-typ_H/K-transp_N.
IPR005775. ATPase_P-typ_Na/K_IIC.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF09040. H-K_ATPase_N. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATP4A_RAT
AccessionPrimary (citable) accession number: P09626
Secondary accession number(s): P70511 expand/collapse secondary AC list , P97892, Q63253, Q6LD86
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families